Structural insights into the human Prostaglandin E receptor EP3-Gi signaling complex
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ABSTRACT:
SUBMITTER: Ryoji Suno
PROVIDER: EMPIAR-11119 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural insights into the G protein selectivity revealed by the human EP3-G<sub>i</sub> signaling complex.
Suno Ryoji R Sugita Yukihiko Y Morimoto Kazushi K Takazaki Hiroko H Tsujimoto Hirokazu H Hirose Mika M Suno-Ikeda Chiyo C Nomura Norimichi N Hino Tomoya T Inoue Asuka A Iwasaki Kenji K Kato Takayuki T Iwata So S Kobayashi Takuya T
Cell reports 20220901 11
Prostaglandin receptors have been implicated in a wide range of functions, including inflammation, immune response, reproduction, and cancer. Our group has previously determined the crystal structure of the active-like EP3 bound to its endogenous agonist, prostaglandin E<sub>2</sub>. Here, we present the single-particle cryoelectron microscopy (cryo-EM) structure of the human EP3-G<sub>i</sub> signaling complex at a resolution of 3.4 Å. The structure reveals the binding mode of G<sub>i</sub> to ...[more]
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